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Database: UniProt
Entry: A0A124I4V1_9ACTN
LinkDB: A0A124I4V1_9ACTN
Original site: A0A124I4V1_9ACTN 
ID   A0A124I4V1_9ACTN        Unreviewed;       547 AA.
AC   A0A124I4V1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=AQJ66_08370 {ECO:0000313|EMBL:KUN87975.1};
OS   Streptomyces bungoensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN87975.1, ECO:0000313|Proteomes:UP000053024};
RN   [1] {ECO:0000313|EMBL:KUN87975.1, ECO:0000313|Proteomes:UP000053024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN87975.1,
RC   ECO:0000313|Proteomes:UP000053024};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT   for the species Streptomyces bungoensis.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006637}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUN87975.1}.
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DR   EMBL; LMWX01000013; KUN87975.1; -; Genomic_DNA.
DR   RefSeq; WP_061919353.1; NZ_KQ948853.1.
DR   AlphaFoldDB; A0A124I4V1; -.
DR   STRING; 285568.AQJ66_08370; -.
DR   OrthoDB; 3713880at2; -.
DR   Proteomes; UP000053024; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd18029; DEXHc_XPB; 1.
DR   CDD; cd18789; SF2_C_XPB; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032830; XPB/Ssl2_N.
DR   PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR   PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR   Pfam; PF16203; ERCC3_RAD25_C; 1.
DR   Pfam; PF13625; Helicase_C_3; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   PRINTS; PR00851; XRODRMPGMNTB.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:KUN87975.1};
KW   Helicase {ECO:0000313|EMBL:KUN87975.1};
KW   Hydrolase {ECO:0000313|EMBL:KUN87975.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:KUN87975.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053024}.
FT   DOMAIN          189..343
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          397..543
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   547 AA;  61021 MW;  AFE52977B732D361 CRC64;
     MNGPLIVQSD KTLLLEVDHE RADDCRRAIA PFAELERAPE HIHTYRVTPL GLWNARAAGH
     DAEQVVDALV QYSRYPVPHA LLVDIAETMD RYGRLTLSKH PAHGLVLTTT DRPVLEEVLK
     SRRIAPLVGA RIDPDTVAVH PSERGQIKQT LLKLGWPAED LAGYVDGEAH PIELVEDGWA
     LRPYQKQAVE NFWHGGSGVV VLPCGAGKTL VGAGSMAQAK STTLILVTNT VSARQWKHEL
     VKRTSLTEDE IGEYSGTRKE IRPVTIATYQ VLTTRRKGVY PHLELFDSRD WGLILYDEVH
     LLPAPVFKFT ADLQARRRLG LTATLVREDG RESDVFSLIG PKRFDAPWKE IEAQGYIAPA
     DCVEVRVNLT DSERLAYATA ETEEKYRFCA TTATKRKVTE ALVRRFAGQQ ILVIGQYIDQ
     LDELGEHLNA PVIKGETSNA QREKLFDAFR EGEISVLVVS KVANFSIDLP EATVAIQVSG
     TFGSRQEEAQ RLGRVLRPKA DGHQAHFYSV VARDTLDQDF AAHRQRFLAE QGYAYRIMDA
     DEILADG
//
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